Anaspec is offering custom synthesis of hydrocarbon-stapled peptides.
Hydrocarbon-stapled peptides are capable of forming stable alpha-helical structures as a result of hydrocarbon stapling.
Many biological pathways, such as signal transduction, occur because of intracellular protein-protein interactions, which are frequently mediated by the a-helix structures of proteins.
However, the use of short protein fragments (peptides) leads to a loss of secondary structure, which makes them susceptible to proteolysis and impermeable across cell membrane.
These problems could be overcome by a chemical modification of an alpha-helical peptide they termed hydrocarbon-stapled peptide.
The modified hydrocarbon-stapled peptide is helical, relatively protease resistant, cell-permeable and binds with increased binding affinity to its target.
Hydrocarbon stapling may provide a useful strategy in researching experimental and therapeutic modulation of protein-protein interactions as well as in in vivo pharmacokinetics studies.
In addition to offering stapled peptides [(i and i+4) and (i and i+7)] custom synthesis service, Anaspec offers Fmoc amino acids for use in synthesising stapled peptides, as well as three GO stapled peptides.
